Identification of grass-specific enzyme that acylates monolignols with p-coumarate |
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Authors: | Withers Saunia Lu Fachuang Kim Hoon Zhu Yimin Ralph John Wilkerson Curtis G |
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Institution: | Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824, USA. |
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Abstract: | Lignin is a major component of plant cell walls that is essential to their function. However, the strong bonds that bind the various subunits of lignin, and its cross-linking with other plant cell wall polymers, make it one of the most important factors in the recalcitrance of plant cell walls against polysaccharide utilization. Plants make lignin from a variety of monolignols including p-coumaryl, coniferyl, and sinapyl alcohols to produce the three primary lignin units: p-hydroxyphenyl, guaiacyl, and syringyl, respectively, when incorporated into the lignin polymer. In grasses, these monolignols can be enzymatically preacylated by p-coumarates prior to their incorporation into lignin, and these monolignol conjugates can also be "monomer" precursors of lignin. Although monolignol p-coumarate-derived units may comprise up to 40% of the lignin in some grass tissues, the p-coumarate moiety from such conjugates does not enter into the radical coupling (polymerization) reactions of lignification. With a greater understanding of monolignol p-coumarate conjugates, grass lignins could be engineered to contain fewer pendent p-coumarate groups and more monolignol conjugates that improve lignin cleavage. We have cloned and expressed an enzyme from rice that has p-coumarate monolignol transferase activity and determined its kinetic parameters. |
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Keywords: | Biofuel Enzyme Kinetics NMR Plant Biochemistry Plant Cell Wall BAHD Acyltransferase Oryza sativa Lignin Monolignol Acylation |
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